Evidence map›Paper›PMID 33392964›Full record

ArticleMolecular diversity2021

Exploring the dynamic mechanism of allosteric drug SHP099 inhibiting SHP2

Shan Du, Xin-Hua Lu, Wei-Ya Li, Li-Peng Li, Yang-Chun Ma, Liang Zhou, Jing-Wei Wu, Ying Ma, Run-Ling Wang

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular diversity, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 42% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Shan DuTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Xin-Hua Lu *New Drug Research & Development Center of North China Pharmaceutical Group Corporation, Key Laboratory for New Drug Screening Technology of Shijiazhuang City, National Microbial Medicine Engineering & Research Center, Hebei Industry Microbial Metabolic Engineering & Technology Research Center, Shijiazhuang, 050015, Hebei, China.
Wei-Ya Li *Tianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Li-Peng LiTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Yang-Chun MaTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Liang ZhouTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Jing-Wei WuTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China.
Ying MaTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China. maying@tmu.edu.cn.
Run-Ling WangTianjin Key Laboratory On Technologies Enabling Development of Clinical Therapeutics and Diagnostics (Theranostics), School of Pharmacy, Tianjin Medical University, Tianjin, 300070, China. wangrunling@tmu.edu.cn.
Tianjin Medical University · CN

Funding

National Natural Science Foundation of China 81773569Natural Science Foundation of Tianjin City 18JCQNJC13700the Science & Technology Development Fund of Tianjin Education Commission for Higher Education 2017KJ229
6 · The paper itself

Abstract

The E69K mutation is one of the most frequent protein tyrosine phosphatase-2 (SHP2) mutations in leukemia, and it can cause the increase in the protein activity. Recent studies have shown that the E69K mutation was fairly sensitive to the allosteric inhibitor of SHP2 (SHP099). However, the molecular mechanism of the allosteric drug SHP099 inhibiting SHP2

Indexed as

Allosteric RegulationMolecular Docking SimulationMolecular Dynamics SimulationDrug StabilityHydrogen BondingMolecular StructurePiperidinesProtein ConformationProtein Tyrosine Phosphatase, Non-Receptor Type 11PyrimidinesStructure-Activity RelationshipPiperidinesProtein Tyrosine Phosphatase, Non-Receptor Type 11PTPN11 protein, humanPyrimidinesSHP099Allosteric inhibitor SHP099E69K mutationMolecular dynamic simulationPost-dynamics analysesProtein tyrosine phosphatase-2

Identifiers

PMID33392964
OpenAlexW3119637977

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.